DOI: 10.1002/bip.1973.360120914. The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents

The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents

10.1002/bip.1973.360120914

Crossref journal-article

Wiley

Biopolymers (311)

Abstract

AbstractRibosomal proteins L7 and L12 are the only acidic proteins found on the 50S ribosomal subunit of Escherichia coli. The effect of ionic strength, helix‐promoting solvents and denaturating agents on the conformation of these proteins has been studied. It has been established that the helicity of L7 and L12 proteins (approx. 45–50% α helix) can be increased to 60–70% when they are exposed to helix‐promoting solvents such as methanol or ethanol in the presence of 0.1M salt. High ionic strength by itself was without any effect on the conformation of the proteins. However, the solvent, 2,2,2‐trifluoroethanol increased the content of α helices up to 80% even in the absence of salt. Denaturating agents like urea (6M) or guanidine HCl (6M), decreased the content of the ordered structure below 20%. All conformational changes induced by salt or solvents were completely reversible and characterized by a broad transition showing a low degree of cooperativity. This might indicate the presence of discrete segments with variations in amino acid sequences and ordered structures with different stabilities.

Bibliography

Boublik, M., Brot, N., & Weissbach, H. (1973). The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents. Biopolymers, 12(9), 2083â2092. Portico.

Authors 3

Miloslav Boublik (first)
Nathan Brot (additional)
Herbert Weissbach (additional)

References 31 Referenced 18

10.1016/0014-5793(70)80261-7
10.1016/0014-5793(70)80262-9
10.1111/j.1432-1033.1972.tb01660.x
10.1111/j.1432-1033.1972.tb01661.x
10.1007/BF00267698
10.1016/0003-9861(72)90125-7
10.1073/pnas.69.8.2120
10.1016/S0021-9258(19)45679-2
10.1038/newbio233062a0
10.1111/j.1432-1033.1972.tb01864.x
10.1111/j.1432-1033.1971.tb01585.x
10.1007/BF00269135
10.1016/0014-5793(72)80742-7
10.1016/0006-291X(70)90960-5
10.1016/S0021-9258(19)52451-6
10.1016/S0003-9861(73)80023-2
10.1007/978-3-662-12641-7
10.1093/oxfordjournals.jbchem.a128704 / J. Biochem. (Tokyo) by Hashizume M. (1967)
10.1021/bi00840a007
10.1021/bi00838a031
10.1002/ange.19650771903
10.1038/222426a0
10.1111/j.1432-1033.1969.tb00535.x
{'key': 'e_1_2_1_25_2', 'volume-title': 'Poly‐α‐Amino Acids', 'author': 'Fasman G. D.', 'year': '1967'} / Poly‐α‐Amino Acids by Fasman G. D. (1967)
{'key': 'e_1_2_1_26_2', 'first-page': '106', 'volume-title': 'Theory of Helix‐Coil Transitions in Biopolymers', 'author': 'Poland D.', 'year': '1970'} / Theory of Helix‐Coil Transitions in Biopolymers by Poland D. (1970)
10.1111/j.1432-1033.1970.tb00845.x
10.1016/S0065-3233(08)60420-9
10.1111/j.1432-1033.1970.tb01147.x
10.1002/bip.1973.360120406
10.1016/0022-2836(73)90030-2
10.1016/0022-2836(69)90238-1

Dates

Type	When
Created	20 years, 7 months ago (Dec. 29, 2004, 8:02 p.m.)
Deposited	1 year, 9 months ago (Nov. 12, 2023, 6:01 a.m.)
Indexed	1 year, 9 months ago (Nov. 23, 2023, 3:53 a.m.)
Issued	51 years, 11 months ago (Sept. 1, 1973)
Published	51 years, 11 months ago (Sept. 1, 1973)
Published Online	21 years, 6 months ago (Feb. 1, 2004)
Published Print	51 years, 11 months ago (Sept. 1, 1973)

Funders 0

None

BibTeX

@article{Boublik_1973, title={The conformational stability of ribosomal proteins L7 and L12 from E. coli. I. Circular dichroism study of the changes induced by ionic strength and solvents}, volume={12}, ISSN={1097-0282}, url={http://dx.doi.org/10.1002/bip.1973.360120914}, DOI={10.1002/bip.1973.360120914}, number={9}, journal={Biopolymers}, publisher={Wiley}, author={Boublik, Miloslav and Brot, Nathan and Weissbach, Herbert}, year={1973}, month=sep, pages={2083–2092} }

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